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Database: UniProt
Entry: G5ZZA4_9PROT
LinkDB: G5ZZA4_9PROT
Original site: G5ZZA4_9PROT 
ID   G5ZZA4_9PROT            Unreviewed;       295 AA.
AC   G5ZZA4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN   ORFNames=HIMB100_00013630 {ECO:0000313|EMBL:EHI47789.1};
OS   SAR116 cluster alpha proteobacterium HIMB100.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX   NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI47789.1, ECO:0000313|Proteomes:UP000004261};
RN   [1] {ECO:0000313|EMBL:EHI47789.1, ECO:0000313|Proteomes:UP000004261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX   PubMed=22675578; DOI=10.4056/sigs.1854551;
RA   Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA   D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA   Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA   Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA   Kyrpides N.C., Rappe M.S.;
RT   "Draft genome sequence of strain HIMB100, a cultured representative of the
RT   SAR116 clade of marine Alphaproteobacteria.";
RL   Stand. Genomic Sci. 5:269-278(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHI47789.1}.
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DR   EMBL; AFXB01000010; EHI47789.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5ZZA4; -.
DR   STRING; 909943.HIMB100_00013630; -.
DR   PATRIC; fig|909943.3.peg.1391; -.
DR   eggNOG; COG0752; Bacteria.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000004261; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   NCBIfam; TIGR00388; glyQ; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Reference proteome {ECO:0000313|Proteomes:UP000004261}.
SQ   SEQUENCE   295 AA;  33323 MW;  527763172F20F316 CRC64;
     MKTDFQSIIL NLQRYWADQG CVILQPYDME VGAGTFHPAT TLRALGPDAV WKAAYVQPSR
     RPTDGRYGEN PNRLQHYYQF QTIMKPSPPD SQQLYLGSLA AIGLDVHAHD IRFVEDDWES
     PTLGAWGLGW EVWCDGMEIS QFTYFQQVGG LECSPVPLEL TYGLERLAMF IQGVENVYDL
     DWDGVPADQG GKSYGDIFHR AEVEFSAWNF EHASTDTLFQ HFRDAEAECR LLLDQQLALP
     AYDQCMKASH LFNLLDARGV ISVSERQAYI GRVRTLAKGC CEAWVGQASI QEPRA
//
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